نتایج جستجو برای: transferases

تعداد نتایج: 3562  

Journal: :The Biochemical journal 1995
C D Hsiao E O Martsen J Y Lee S P Tsai M F Tam

Glutathione S-transferase CL1-2 heterodimers purified from 1-day-old chick livers were digested with Achromobacter proteinase I. The resulting fragments were separated for amino acid sequence analysis. Oligonucleotide probes were constructed based on sequence similarity to class-Theta glutathione S-transferases for PCR using a chicken liver cDNA library as template. A full-length clone (1725 bp...

2003
Miguel A. Valvano

1. Abstract 2. Introduction 3. Biogenesis of O-specific lipopolysaccharides 3.1. Initiation reaction 3.1.1. Polyisoprenyl-phosphate N-acetylhexosamine-1-phosphate transferases 3.1.2. Polyisoprenyl-phosphate hexose-1-phosphate transferases 3.2. Elongation/translocation/polymerization 3.2.1. Wzy/Wzx-dependent pathway 3.2.2. ABC transporter pathway 3.2.3. Synthase pathway 3.3. Ligation reaction 3....

2005
Thomas D. HONG Yogesh C. AWASTHI

Human brain contains one cationic (pI8.3) and two anionic (pI5.5 and 4.6) forms of glutathione S-transferase. The cationic form (pI 8.3) and the less-anionic form (p1 5.5) do not correspond to any of the glutathione S-transferases previously characterized in human tissues. Both of these forms are dimers of 26 500-Mr subunits; however, immunological and catalytic properties indicate that these t...

Journal: :Glycobiology 2003
Leo Kinarsky Ganesh Suryanarayanan Om Prakash Hans Paulsen Henrik Clausen Franz-Georg Hanisch Michael A Hollingsworth Simon Sherman

The tandem repeat of the MUC1 protein core is a major site of O-glycosylation that is catalyzed by several polypeptide GalNAc-transferases. To define structural features of the peptide substrates that contribute to acceptor substrate efficiency, solution structures of the 21-residue peptide AHGVTSAPDTRPAPGSTAPPA (AHG21) from the MUC1 protein core and four isoforms, glycosylated with alpha-N-ace...

2005
Shivendra V. SINGH Catherine A. PARTRIDGE Yogesh C. AWASTHI

Two immunologically distinct types of 22000-Mr subunits are present in rat lung glutathione S-transferases. One of these subunits is probably similar to Ya subunits of rat liver glutathione S-transferases, whereas the other subunit Ya' is immunologically distinct. Glutathione S-transferase II (pI7.2) of rat lung is a heterodimer (YaYa') of these subunits, and glutathione S-transferase VI (pI4.8...

Journal: :The Journal of biological chemistry 1982
J A Redick W B Jakoby J Baron

Sheep antibodies raised against three isoenzymes of glutathione S-transferase (EC 2.5.1.18), transferases B, C, and E, which were isolated and purified to apparent homogeneity from rat liver, have been employed to localize these enzymes at the light microscopic level within livers of untreated rats. Using these antibodies in an unlabeled antibody peroxidase-antiperoxidase staining technique, ea...

Journal: :RNA 2007
Georges Martin Walter Keller

RNA-specific nucleotidyl transferases (rNTrs) are a diverse family of template-independent polymerases that add ribonucleotides to the 3'-ends of RNA molecules. All rNTrs share a related active-site architecture first described for DNA polymerase beta and a catalytic mechanism conserved among DNA and RNA polymerases. The best known examples are the nuclear poly(A) polymerases involved in the 3'...

2006
Vladimir N. Shibaev

An approach to the study of the specificity of glycosyl transferases is discussed which is based on the use of synthetic substrate analogs. A new method has been developed for the synthesis of polyprenyl pyrophosphate sugars, intermediates in the biosynthesis ofSalmonella 0-specific polysaccharides. Some synthetic analogs of guanosine diphosphate D-mannose and thymidine diphosphate L-rhamnose h...

Journal: :The Biochemical journal 1985
U H Danielson B Mannervik

The steady-state kinetics of the dimeric glutathione transferases deviate from Michaelis-Menten kinetics, but have hyperbolic binding isotherms for substrates and products of the enzymic reaction. The possibility of subunit interactions during catalysis as an explanation for the rate behaviour was investigated by use of rat isoenzymes composed of subunits 1, 2, 3 and 4, which have distinct subs...

Journal: :The Journal of biological chemistry 1997
H H Wandall H Hassan E Mirgorodskaya A K Kristensen P Roepstorff E P Bennett P A Nielsen M A Hollingsworth J Burchell J Taylor-Papadimitriou H Clausen

Mucin-type O-glycosylation is initiated by UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). The role each GalNAc-transferase plays in O-glycosylation is unclear. In this report we characterized the specificity and kinetic properties of three purified recombinant GalNAc-transferases. GalNAc-T1, -T2, and -T3 were expressed as soluble proteins in inse...

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